As biochemical methods for production of aromatic D-amino Acid, a known method comprises contacting DL-allylmethylhydantoin with a microorganism capable of selectively hydrolyzing D-allylmethylhydantoin to N-carbamoyl-D-amino acid to synthesize N-carbamoyl-D-amino acid and hydrolyzing N-carbamoyl-D-amino acid to D-amino acid chemically, for example, with nitrous acid, or using a microorganism to produce D-amino acid (hydantoinase method, JP-A-Sho 61-17791).
It is also known to produce D-amino acid by a method comprising contacting DL-amino acid amide with a microorganism or enzyme capable of selectively hydrolyzing D-amino acid amide alone in DL-amino acid amide (D-amidase method, JP-B-Hei 08-22228) and a method comprising selectively hydrolyzing L-amino acid amide alone in DL-amino acid amide and chemically hydrolyzing the remaining D-amino acid amide (L-amidase method, JP-A-Sho 57-13000).
Further, other known methods of producing D-amino acid include a method comprising contacting indole pyruvic acid, phenyl pyruvic acid, and the like and D-alanine as an amino group donor with D-amino acid transaminase (transaminase method, JP-B-Hei 07-85718), a method comprising contacting N-acetyl-DL-amino acid with L-aminoacylase capable of selectively deacetylating N-acetyl-L-amino acid and chemically deacetylating remaining N-acetyl-D-amino acid (L-aminoacylase method, Methods in Enzymology 3, 554-570 (1957)), a method comprising contacting N-acetyl-D-amino acid with D-aminoacylase capable of selectively deacetylating N-acetyl-DL-amino acid (D-aminoacylase method, JP-B-Hei 01-29560), and a method comprising contacting DL-amino acid with D-amino acid acetyltransferase to selectively convert D-amino acid to N-acetyl-D-amino acid and, after separation from the remaining L-amino acids, chemically hydrolyzing N-acetyl-D-amino acid thus formed (acetyltransferase method, JP-A-Sho 60-251892).
On the other hand, as methods for biochemical production of aromatic amine, there have been reported a method comprising decarboxylation of L-tyrosine using tyrosine decarboxylase derived from microorganism belonging to the genus Streptococcus to obtain tyramine (JP-A-Sho 55-102393), a similar method to the above by which dopamine is obtained from L-dopa (JP-A-Sho 55-102394), a method of producing amine from the corresponding amino acid using aromatic amino acid decarboxylase derived from the genus Micrococcus belonging to bacteria (Nakazawa, H. et al., Biosci. Biotechnol. Biochem. 57(7), 1210-1211(1993)), and a method of obtaining amine from the corresponding aromatic amino acid using a microorganism belonging to the genus Staphylococcus (JP-A-Sho 50-155689).
Aromatic amino acid decarboxylases are known to be distributed among mammals, insects, plants, and microorganisms. However, regarding those derived from microorganisms, only aromatic amino acid decarboxylase derived from microorganisms belonging to the genus Micrococcus (Nakazawa, H. et al., Biosci. Biotechnol. Biochem. 57(7), 1210-1211(1993)), aromatic amino acid decarboxylase derived from Pholiota nameko (JP-A-Sho 61-234780), and microorganisms belonging to the genus Staphylococcus (JP-A-Sho 50-155689) have been reported to have aromatic amino acid decarboxylating activity. At present, there is no report that fungi belonging to the genera Fusarium, Gibberella, Aspergillus, Pleurotus, Nectria, and the like have aromatic amino acid decarboxylase. There is also no report of production of aromatic D-amino acid and corresponding amine from a mixture of enantiomers of aromatic amino acid using microorganisms belonging to these genera. Some microorganisms belonging to the genus Fusarium are reported to have phenylalanine decarboxylase activity (Ferencik M. and Ladzianska K., Folia Microbiology 13, 414-418 (1968)). This report describes that the amino acid decarboxylation reaction was limitedly carried out within pH 4.6-5.6 and that the microorganisms did not act on tryptophan and tyrosine. Further, there is no description in this report of the use of microorganism for selective degradation of L-amino acid to produce D-amino acid.
Thus, concerning the microorganisms belonging to the genera Fusarium, Gibberella, Aspergillus, Pleurotus, Nectria, it has not been reported so far that various aromatic amino acids, especially the L-form thereof, are selectively decarboxylated to form the corresponding amines and that selective degradation of L-amino acid results in a remarkable increase in the content of D-amino acid in the reaction system.
Further, the above-described conventional methods have drawbacks for industrial production of aromatic D-amino acid and amine because the substrates are expensive, the reaction steps are complicated, the yield is low, and the optical purity of the product is low.